Information on EC 1.3.1.24 - biliverdin reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.1.24
-
RECOMMENDED NAME
GeneOntology No.
biliverdin reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
heme degradation I
-
-
heme metabolism
-
-
Porphyrin and chlorophyll metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
bilirubin:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9074-10-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Syncerus sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
using BVR siRNA, blocking generation of bilirubin, reverses the effect of hypoxia on enhancing cell survival and apoptotic protein (Bcl-2, procasepase-9, procasepase-3) expression, preventing nuclear shrinkage, DNA fragmentation and mitochondrial depolarization in starved pulmonary arterial smooth muscle cell, which are recovered by exogenous bilirubin. The inhibitory effect of bilirubin on pulmonary arterial smooth muscle cell apoptosis under hypoxic condition is blocked by the inhibitor of ERK1/2 pathway
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Akt protein + NAD(P)H
?
show the reaction diagram
-
-
-
-
-
?
bilirubin + NAD(P)+
biliverdin + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
show the reaction diagram
bilirubin + NADP+
biliverdin + NADPH + H+
show the reaction diagram
bilirubin-IXa + NAD+
biliverdin-IXa + NADH + H+
show the reaction diagram
-
-
-
-
-
bilirubin-IXa + NADP+
biliverdin-IXa + NADPH + H+
show the reaction diagram
-
-
-
-
-
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
show the reaction diagram
biliverdin + NAD(P)H
bilirubin + NAD(P)+
show the reaction diagram
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
show the reaction diagram
biliverdin + NADH + H+
bilirubin + NAD+
show the reaction diagram
biliverdin + NADPH + H+
bilirubin + NADP+
show the reaction diagram
biliverdin IXalpha + NAD(P)H
bilirubin + NAD(P)+
show the reaction diagram
-
-
-
-
?
biliverdin IXalpha + NAD(P)H + H+
bilirubin + NAD(P)+
show the reaction diagram
-
-
-
-
?
biliverdin IXalpha + NAD(P)H + H+
bilirubin IXalpha + NAD(P)+
show the reaction diagram
biliverdin IXalpha + NADH + H+
bilirubin IXalpha + NAD+
show the reaction diagram
-
substrate for isoform BVRA
-
-
r
biliverdin IXalpha + NADPH + H+
bilirubin IXalpha + NADP+
show the reaction diagram
-
substrate for isoform BVRA
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin + NAD+
show the reaction diagram
-
-
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin IXbeta + NAD+
show the reaction diagram
-
substrate for isoform BVRB
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin + NADP+
show the reaction diagram
-
-
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin IXbeta + NADP+
show the reaction diagram
-
substrate for isoform BVRB
-
-
r
casein + NAD(P)H
?
show the reaction diagram
-
BVR functions as an serine/threonine kinase for casein
-
-
?
Elk-1 protein + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
extracellular signal-regulated kinase 1 + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
extracellular signal-regulated kinase 2 + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
insulin receptor substrate 1 + NAD(P)H
?
show the reaction diagram
insulin receptor substrate-1 + NAD(P)H
?
show the reaction diagram
-
the serine residues are targets for BVR phosphorylation
-
-
?
insulin-receptor substrate 1 + NAD(P)H
?
show the reaction diagram
-
BVR functions as an serine/threonine kinase for insulin-receptor substrate 1
-
-
?
mitogen-activated protein kinase kinase 1 + NAD(P)H
?
show the reaction diagram
-
-
-
-
?
myelin basic protein + NAD(P)H
?
show the reaction diagram
-
BVR functions as an serine/threonine kinase for myelin basic protein
-
-
?
phosphatidylinositol 3-kinase + NAD(P)H
?
show the reaction diagram
-
-
-
-
-
?
protein kinase C-betaII + NAD(P)H
?
show the reaction diagram
-
BVR functions as an serine/threonine kinase for protein kinase C-betaII
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bilirubin + NAD(P)+
biliverdin + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
show the reaction diagram
bilirubin + NADP+
biliverdin + NADPH + H+
show the reaction diagram
bilirubin-IXa + NAD+
biliverdin-IXa + NADH + H+
show the reaction diagram
-
-
-
-
-
bilirubin-IXa + NADP+
biliverdin-IXa + NADPH + H+
show the reaction diagram
-
-
-
-
-
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
show the reaction diagram
biliverdin + NAD(P)H
bilirubin + NAD(P)+
show the reaction diagram
biliverdin + NADH + H+
bilirubin + NAD+
show the reaction diagram
biliverdin + NADPH + H+
bilirubin + NADP+
show the reaction diagram
biliverdin IXalpha + NAD(P)H + H+
bilirubin + NAD(P)+
show the reaction diagram
-
-
-
-
?
biliverdin IXalpha + NADH + H+
bilirubin IXalpha + NAD+
show the reaction diagram
-
substrate for isoform BVRA
-
-
r
biliverdin IXalpha + NADPH + H+
bilirubin IXalpha + NADP+
show the reaction diagram
-
substrate for isoform BVRA
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin + NAD+
show the reaction diagram
-
-
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin IXbeta + NAD+
show the reaction diagram
-
substrate for isoform BVRB
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin + NADP+
show the reaction diagram
-
-
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin IXbeta + NADP+
show the reaction diagram
-
substrate for isoform BVRB
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
-
-
Zn2+
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
albumin
-
-
-
Arsenobenzoate
-
1 mM, slight
bilirubin
Biliverdin
biliverdin IXalpha
-
with cofactor NADPH, inhibitory above 0.004 mM, with cofactor NADH, inhibitory above 0.018 mM
Ca2+
-
abolishes autophosphorylation of BVR
Dithionitrobenzoate
-
-
FAD
-
-
FMN
-
-
GATA1
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transcription factor GATA1 downregulates BVR expression
-
HgCl2
-
irreversible inhibition
iodoacetamide
iodoacetate
-
-
Iron-hematoporphyrin
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competitive, acts as biliverdin-bilirubin analog
lipase
-
-
-
Metalloporphyrin complexes
-
-
-
Mg2+
-
abolishes autophosphorylation of BVR
N-ethylmaleimide
NADH
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at pH 8.5, competitive to NADPH
NADP+
NADPH
-
at pH 7.0, competitive to NADH
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
-
potato acid phosphatase
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human bilverdin reductase expressed in E. coli
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Protein phosphatase 2A
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human bilverdin reductase expressed in E. coli, okadaic acid attenuates the inhibition
-
SH-reactive agent
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34000 Da form extremely sensitive to, larger 68000 Da form lacks sensitivity to
-
SH-reagents
-
siRNA
-
Trypsin
-
-
-
zinc-protoporphyrin
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-
Zn2+
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inhibitory to autophosphorylation of BVR, can not be overcome with Mn2+
additional information
-
since no specific inhibitors for BVR are known, siRNA is used to silence the BVR gene in primary endothelial cells and accordingly suppress its activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
-
cGMP
-
BVR localizes into the nucleus upon activation by cGMP
Co-protoporphyrin complex
-
activates
cobalt protoporphyrin
-
activates
cytokine
-
induces BVR transcription
-
Fe-protoporphyrin complex
-
activates
Ferredoxin
-
-
-
heme
-
upregulates BVR expression
hyperthermia
-
induces BVR transcription
-
Insulin
-
increases BVR tyrosine autophosphorylation
-
oxidant
-
Tumor necrosis factor alpha
-
-
-
Urea
-
the enzyme is activated at low concentrations of urea
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 0.1633
Biliverdin
0.0004 - 0.023
biliverdin IXalpha
0.107 - 2
NADH
0.001 - 0.059
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 94.8
Biliverdin
1.7 - 5.6
NADH
0.01 - 0.4
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 15100
Biliverdin
1.7 - 21
NADPH
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026 - 0.0117
bilirubin
0.028 - 0.147
Biliverdin
0.0019 - 1.7
NAD+
0.00035 - 0.583
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
-
HeLa cells transfected with BVR-targeted RNAi
0.00035
-
BVR activity in HeLa cells, control
0.00075
-
HeLa cells transfected with pcDNA3-BVR, overexpression of BVR
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
cosubstrate NADPH
5.8
-
biliverdin + NADPH
6.9
-
biliverdin + NADH
7.3
-
activity assay
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
biliverdin + NADPH, pH 6: about 50% of activity maximum, pH 9: 27% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
-
exposure of male rats to 42°C for 20 min does not decrease brain biliverdin activity, the 1.5 kb biliverdin reductase mRNA displayes thermal tolerance too
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
Syncerus sp.
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
shows increased BVR level
Manually annotated by BRENDA team
-
increased activity of BVR, but only in the presence of NADH
Manually annotated by BRENDA team
-
pulmonary arterial smooth muscle cell
Manually annotated by BRENDA team
-
inflamed lesions, increased in rats with clinical autoimmune encephalomyelitis, also present in both white and gray matter
Manually annotated by BRENDA team
-
sparingly expressed
Manually annotated by BRENDA team
additional information
-
the BVR activity progressively increases after birth and reaches adult levels by postpartum day 28
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30100
-
SDS-PAGE
30400 - 31400
-
various forms, two dimensional PAGE
32000
-
gel filtration; kidney, gel filtration
34000 - 36000
-
liver
34600
-
1 * 39900 + 1 * 34600, in vitro translated proteins, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
38000
-
the HY2 gene encodes a soluble protein precursor with a putative N-terminal plastid transit peptide, this protein is phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase, SDS-PAGE
39900
-
1 * 39900 + 1 * 34600, in vitro translated proteins, SDS-PAGE
41000 - 42000
-
the purified protein resolves into two molecular weight forms of 40700 and 39600, two-dimensional electrophoresis
54000
-
liver (form 2), HPLC
56000
-
minor form 2, SDS-PAGE
60000
-
expression of rat biliverdin reductase as a gluthatione-S-transferase protein, SDS-PAGE
69000
-
in vitro translated reductase, 12% native polyacryamide gel
70000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50 mM Tris-HCl (pH 7.25), 0.2 M sodium acetate and 0.2 mM Cymal-2
-
hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.2M MgCl2 and 0.1 M BisTris at pH 5.5
-
apo enzyme and in complex with NADH
-
apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
BVR-NADH complex, NH2-terminal domain in dinucleotide binding
-
crystals of the biliverdin reductase obtained by sitting-drop vapour-diffusion method, enzyme diffraction data collected to 1.6 A, crystals belong to the orthorhombic space group P212121 with unit-cell parameters a=58.89, b=70.41, c=87.76 A
-
an X-ray diffraction experiment using a native BVR crystal is performed on the BL38B1 beamline. The crystal belongs to the orthorhombic space group P2-1-2-1-2-1, with unit-cell parameters a = 58.8, b = 88.4, c = 132.6 A. A complete data set is collected to a resolution of 2.34 A
-
apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
0.1 M potassium phosphate buffer, most stable
437789
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
10 min, no loss of activity
55
-
10 min, complete loss of activity
56
-
5 min, complete loss of activity
60
-
1 h, 15-30% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity in solutions with protein concentration below 0.030-0.035 mg/ml
-
NADPH stabilizes
-
repeated freeze-thawing: little loss of activity , no significant loss of activity, partially purified enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate, pH 7.0, stable for at least eight months
-
-20°C, 8 weeks, 1-10 mg protein per ml, 5-25% loss of activity, partially purified enzyme
-
-20°C, several months -25°C, 1 month: no loss of activity, 2 months: 50% loss of activity
0-4°C, 5 days
-
0°C, 8 weeks, 1-10 mg protein per ml, 15-25% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinitiy chromatography
-
CNBr-activated Sepharose column chromatography, and Superdex 200 gel filtration
-
glutathione-Sepharose column chromatography, and Superdex 200 gel filtration
-
Ni-NTA agarose column chromatography
-
Ni-NTA resin column chromatography, HisTrap column chromatography and Superdex 75 gel filtration
-
nickel affinity gel chromatography and Sephacryl S-200 gel filtration
protein extracts of transgenic Arabidopsis thaliana plants are prepared
-
purification of biliverdin reductase expressed in Escherichia coli and from rat tissue
-
using affinity purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
biliverdin reductase cDNA cloned into pUC18, used for expression and purification
-
expressed in Escherichia coli
expressed in Escherichia coli and HeLa cells
-
expressed in Escherichia coli BL-21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-RIL cells
-
expressed in Escherichia coli C41(DE3) cells
expressed in HEK-293 cells
-
expressed in HEK293A and MCF-7 cells
-
expression in H9C2 cell
-
expression in HEK-293A cells
-
expression in SH-SY5Y cells
-
human biliverdin reductase expressed in Escherichia coli
-
into pcDNA3 and expressed in 293A cells pcDNA3, into pGEX4-T2 and expressed in Escherichia coli
-
into the pGEM-T easy vector, subcloned into the vectors pcDNA3 and pESC-LEU
-
into the vector pcDNA3.1
into vector pcDNA3, transformed into Escherichia coli DH5alpha, pGEX-4T2/human BVR vector
-
kidney form of the enzyme cloned into the expression vector pGEX-KG
-
overexpressed in Escherichia coli as a His-tagged fusion protein
-
recombinant biliverdin reductase expressed in Escherichia coli
-
recombinant BVR is used
-
reversible overexpression of BVR in mouse fibroblasts, doxycycline-dependent overexpression of BVR in NIH 3T3 BVR-Tet-On cells confers protection against cytotoxic drugs cisplatin and doxorubicin
-
the expression of rat kidney biliverdin reductase is targeted by translational fusion of the chloroplast transit peptide sequence of the soybean small subunit of ribulose bisphosphate carboxylase gene to the enzyme cDNA, with this method transgenic Arabidopsis plants are cloned which express constitutive biliverdin reductase and display aberrant photomorphogenesis throughout their life-cycle
-
using the vector pBIB-KAN a plant transformation vector, containing the CAB3 promoter, a chloroplast targeting sequence and the BVR gene, is constructed, using pMON672 leads to a similar construct containing the MERI5 promoter
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
about 56% of the BVR expression in total lung tissue is increased by hypoxia; up-regulated in levels of protein and mRNA by hypoxia in pulmonary arterial smooth muscle cell
-
atorvastatin significantly increases BVR-A protein levels, phosphorylation and activity only in parietal cortex
-
bacterial endotoxin, lipopolysaccharide, initiates an inflammatory response in macrophages coming along with a rapid increase in BVR surface expression
BVR expression is unaffected by heat shock
-
BVR is induced by lipopolysaccharides and bromobenzene at a post-transcriptional level
-
doxycycline dose-dependently induces BVR gene expression at the level of mRNA as well as a protein, and BVR activity in genetically modified NIH 3T3 fibroblasts
-
enzyme expression is up-regulated in breast cancer cells
-
hypoxia positively regulates hBVR promoter; overexpression of IkappaB increases hBVR mRNA; TNF-alpha negatively regulates hBVR promoter
-
in fetal liver and maternal liver and placenta ursodeoxycholic acid up-regulates biliverdin-IX reductase
-
in HEK-293A cells, hypoxia modestly increases BVR mRNA levels
-
in HepG2 and JAr cells taurocholic acid and ursodeoxycholic acid up-regulate biliverdin-IX reductase
-
increased expression in macrophages of primary spontaneous pneumothorax of smokers compared to non-smokers; oxidative stress induces HO-1, BVR and H-ferritin in lung macrophages, this is involved in development of primary spontaneous pneumothorax disease, overview. HIF-1alpha siRNA transfection completely abrogated the increased HO-1, BVR and H-ferritin mRNA levels
-
induction of BVR and HO-2 is mediated by the cAMP-PKA pathway and isoproterenol, overview
-
induction of BVR and HO-2 is mediated by the cAMP-PKA pathway and isoproterenol, overview. The beta-adrenergic antagonist propranolol only slightly induces BVR expression in HEK-293A cells
-
patients with chronic hepatitis C virus infection show significantly upregulated enzyme expression in peripheral blood leukocytes
-
the transcript and protein levels are increased in human tumors and the infiltrating T-cells, monocytes and circulating lymphocytes, as well as the circulating and infiltrating macrophages
-
treatment of cultured TALH or IMCD-3 cells with BVR siRNA, 50 or 100 nM, results in an 80% decrease in the level of BVR protein
-
up-regulation is found in the hippocampus of subjects with Alzheimer disease in its earliest form
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C281A/C292A/C293A
H132A
-
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R124A
-
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R172A
-
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R172E
-
inactive
R172K
-
inactive
R174A
-
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R18Stop
R35A
-
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R35S
-
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R39A
-
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
R78A
-
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
S111A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
S111L
-
the mutant shows strongly reduced activity compared to the wild type enzyme
V11A/V12A/V13A/V14A
-
not only fails to activate protein kinase C but also decreases its activity by 22%
W116A
-
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
W116F
-
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
Y198F
-
mutant, phosphorylation site
Y98F
-
the mutant shows about wild type catalytic efficiency
E47A
-
mutant, does affect the edge of the beta2 strand of substrate and cofactor binding in the pocket, which likely influences the strength of their interaction with BVR
E97A
-
mutant, data strongly support this site as important for conversion of biliverdin to bilirubin and for transmission of signaling by BVR
C280A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 280 principally functions in substrate binding
C291A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 291 is predominantly involved in cofactor binding.
C73A
-
the modification of the amino-proximal cysteine, which is flanked by a tyrosine residue, completely inactivates the enzyme with NADH at pH 6.75 and NADPH at pH 8.7
R171A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171E
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y98F
the mutant shows about wild type catalytic efficiency
K237A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R185A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R185K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R188A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R246A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S184A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T169A
the mutant shows wild type catalytic efficiency
Y102F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information